Кафедра биохимии и биотехнологии приглашает вас
17 мая 2018 г. в 11.50 на открытую лекцию
Юсупова Марата Миратовича
Научный руководитель лаборатории НИЛ
Структурная Биология ИФМиБ,
Директор по исследованиям C.N.R.S.,
руководитель лаборатории Структура
рибосомы IGBMC,
в.н.с. НИЛ Структурная биология ИФМиБ
Страсбург, Франция (h-index - 27)
17 мая 2018 г. в 11.50
в ауд. 019 Восточного крыла Главного здания лекция
«Кристаллические структуры эукариотических и бактериальных рибосом»
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Annotation
Ribosomes from bacteria consist of a large and a small subunit, which together compose the 2.5 megadalton (MDa) 70S ribosome. Their eukaryotic counterpart is the 80S ribosome (from 3.5 MDa in lower eukaryotes to 4.5 MDa in higher). Many ribosomal key components are conserved across the three kingdoms of life: bacteria, archaea, and eukarya and constitutes a common core undertaking the fundamental processes of protein biosynthesis.
The complete structure of the full 80S ribosome from Saccharomyces cerevisiae at a resolution of 3Å have been determined. The model includes nearly all the rRNA sequences as well as all ribosomal proteins. The eukaryotic 80S and bacterial 70S ribosome shares 34 common proteins and eukaryotic ribosome has additional 45 unique proteins and bacterial ribosome has 22 additional unique proteins. The majority of eukaryotic specific elements are located on the periphery of the conserved core thus broadening the surface of interactions between the two subunits through additional eukaryotic bridges.
The molecular interactions creating these bridges together with their eukaryotic-specific components now described in details. Our crystals capture the ribosome in two different conformations which are believed to reflect intermediate states in course of mRNA and tRNA translocation. The structural comparison of these states, which differ by the degree of rotation of the small subunit and the swiveling of its head with respect to the large subunit, provides a detailed description of conformational rearrangements as well as coordinated movements of intersubunit bridges. The ribosome is a major target for small-molecule inhibitors. We used X-ray crystallography to determine 16 high-resolution structures of the full 80S ribosome from Saccharomyces cerevisiae in complexes with 12 eukaryote-specific and 4 broad-spectrum inhibitors. All inhibitors were found associated with messenger RNA and transfer RNA binding sites. Our study defines common principles of targeting and resistance, provides insights into their mode of action.
За дополнительной информацией обращаться к заведующей кафедрой биохимии и биотехнологии Киямовой Рамзие Галлямовне, kiyamova@mail.ru; тел.2337440